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Volumn 318, Issue 2, 2004, Pages 353-363

Rat sperm AS-A: Subcellular localization in testis and epididymis and surface distribution in epididymal sperm

Author keywords

Arylsulfatase A; Epididymis; Rat (Wistar); Sperm; Sperm maturation; Testis

Indexed keywords

CEREBROSIDE SULFATASE;

EID: 8644232435     PISSN: 0302766X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00441-004-0985-4     Document Type: Article
Times cited : (8)

References (35)
  • 1
    • 0033037440 scopus 로고    scopus 로고
    • Cell- and region-specific localization of lysosomal and secretory proteins and endocytic receptors in epithelial cells of the cauda epididymidis and vas deferens of the adult rat
    • Andonian S, Hermo L (1999) Cell- and region-specific localization of lysosomal and secretory proteins and endocytic receptors in epithelial cells of the cauda epididymidis and vas deferens of the adult rat. J Androl 20:415-429
    • (1999) J Androl , vol.20 , pp. 415-429
    • Andonian, S.1    Hermo, L.2
  • 2
    • 0029041187 scopus 로고
    • Phosphomannosyl receptors on the surface of spermatozoa from the cauda epididymis of the rat
    • Barbieri AM, Sosa MA, Grimalt P, Mayorga LS, Bertini F (1995) Phosphomannosyl receptors on the surface of spermatozoa from the cauda epididymis of the rat. Int J Androl 18:113-119
    • (1995) Int J Androl , vol.18 , pp. 113-119
    • Barbieri, A.M.1    Sosa, M.A.2    Grimalt, P.3    Mayorga, L.S.4    Bertini, F.5
  • 3
    • 1842414818 scopus 로고    scopus 로고
    • Extraction and quantification of acrosin, β-N-acetylglucosaminidase, and arylsulfatase-A from equine ejaculated spermatozoa
    • Brandon CI, Srivastava PN, Heusner GL, Fayrer-Hosken RA (1997) Extraction and quantification of acrosin, β-N-acetylglucosaminidase, and arylsulfatase-A from equine ejaculated spermatozoa. J Exp Zool 279:301-308
    • (1997) J Exp Zool , vol.279 , pp. 301-308
    • Brandon, C.I.1    Srivastava, P.N.2    Heusner, G.L.3    Fayrer-Hosken, R.A.4
  • 6
    • 0032227096 scopus 로고    scopus 로고
    • Interactions between epididymal secretions and spermatozoa
    • Cooper TG (1998) Interactions between epididymal secretions and spermatozoa. J Reprod Fertil Suppl 53:119-136
    • (1998) J Reprod Fertil Suppl , vol.53 , pp. 119-136
    • Cooper, T.G.1
  • 8
    • 0024364949 scopus 로고
    • Mannose 6-phosphate receptors and lysosomal enzyme targeting
    • Dahms NM, Lobel P, Kornfeld S (1989) Mannose 6-phosphate receptors and lysosomal enzyme targeting. J Biol Chem 264:12115-12118
    • (1989) J Biol Chem , vol.264 , pp. 12115-12118
    • Dahms, N.M.1    Lobel, P.2    Kornfeld, S.3
  • 9
    • 0021215437 scopus 로고
    • Purification of boar acrosomal arylsulfatase A and possible role in the penetration of cumulus cells
    • Dudkiewicz AB (1984) Purification of boar acrosomal arylsulfatase A and possible role in the penetration of cumulus cells. Biol Reprod 30:1005-1014
    • (1984) Biol Reprod , vol.30 , pp. 1005-1014
    • Dudkiewicz, A.B.1
  • 10
    • 0030974131 scopus 로고    scopus 로고
    • AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins
    • Foster JA, Friday BB, Maulit MT, Blobel C, Winfrey VP, Olson GE, Kim KS, Gerton GL (1997) AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins. J Biol Chem 272:12714-12722
    • (1997) J Biol Chem , vol.272 , pp. 12714-12722
    • Foster, J.A.1    Friday, B.B.2    Maulit, M.T.3    Blobel, C.4    Winfrey, V.P.5    Olson, G.E.6    Kim, K.S.7    Gerton, G.L.8
  • 11
    • 0035094384 scopus 로고    scopus 로고
    • Prostasome-like particles are involved in the transfer of P25b from the bovine epididymal fluid to the sperm surface
    • Frenette G, Sullivan R (2001) Prostasome-like particles are involved in the transfer of P25b from the bovine epididymal fluid to the sperm surface. Mol Reprod Dev 59:115-121
    • (2001) Mol Reprod Dev , vol.59 , pp. 115-121
    • Frenette, G.1    Sullivan, R.2
  • 13
    • 0026470144 scopus 로고
    • Characterization of three arylsulfatases in semen: Seminolipid sulfohydrolase activity is present in seminal plasma
    • Gadella BM, Colenbrander B, van Golde LMG, Lopes-Cardozo M (1992) Characterization of three arylsulfatases in semen: seminolipid sulfohydrolase activity is present in seminal plasma. Biochim Biophys Acta 1128:155-162
    • (1992) Biochim Biophys Acta , vol.1128 , pp. 155-162
    • Gadella, B.M.1    Colenbrander, B.2    Van Golde, L.M.G.3    Lopes-Cardozo, M.4
  • 14
    • 0032516869 scopus 로고    scopus 로고
    • Testin secreted by Sertoli cells is associated with the cell surface, and its expression correlates with the disruption of Sertoli-germ cell junctions but not the inter-Sertoli tight junction
    • Grima J, Wong CCS, Zhu L, Zong S, Cheng CY (1998) Testin secreted by Sertoli cells is associated with the cell surface, and its expression correlates with the disruption of Sertoli-germ cell junctions but not the inter-Sertoli tight junction. J Biol Chem 273:21040-21053
    • (1998) J Biol Chem , vol.273 , pp. 21040-21053
    • Grima, J.1    Wong, C.C.S.2    Zhu, L.3    Zong, S.4    Cheng, C.Y.5
  • 15
    • 0028801208 scopus 로고
    • Organ-specific binding system for beta-galactosidase in the male reproductive tract
    • Grimalt P, Barbieri MA, Sosa MA, Bertini F (1995) Organ-specific binding system for beta-galactosidase in the male reproductive tract. Int J Androl 18:243-247
    • (1995) Int J Androl , vol.18 , pp. 243-247
    • Grimalt, P.1    Barbieri, M.A.2    Sosa, M.A.3    Bertini, F.4
  • 16
    • 0001866451 scopus 로고    scopus 로고
    • Epididymal cell types and functions
    • Robaire B, Hinton BT (eds) Kluwer/Plenum, New York
    • Hermo L, Robaire B (2002) Epididymal cell types and functions. In: Robaire B, Hinton BT (eds) The epididymis: from molecule to clinical practice. Kluwer/Plenum, New York, pp 81-102
    • (2002) The Epididymis: From Molecule to Clinical Practice , pp. 81-102
    • Hermo, L.1    Robaire, B.2
  • 17
    • 0028674555 scopus 로고
    • Secretion and endocytosis in the male reproductive tract: A role in sperm maturation
    • Hermo L, Oko R, Morales CR (1994) Secretion and endocytosis in the male reproductive tract: a role in sperm maturation. Int Rev Cytol 154:106-189
    • (1994) Int Rev Cytol , vol.154 , pp. 106-189
    • Hermo, L.1    Oko, R.2    Morales, C.R.3
  • 18
    • 0020446015 scopus 로고
    • 3H] alpha-aminoisobutyric acid across its epithelia in vivo
    • 3H] alpha-aminoisobutyric acid across its epithelia in vivo. Biol Reprod 27:1181-1189
    • (1982) Biol Reprod , vol.27 , pp. 1181-1189
    • Hinton, B.T.1    Howards, S.S.2
  • 19
    • 0024615443 scopus 로고
    • Presence of a lysosomal enzyme, arylsulfatase-A, in the prelysosome-endosome compartments of human cultured fibroblasts
    • Kelly BM, Yu CZ, Chang PL (1989) Presence of a lysosomal enzyme, arylsulfatase-A, in the prelysosome-endosome compartments of human cultured fibroblasts. Eur J Cell Biol 48:71-78
    • (1989) Eur J Cell Biol , vol.48 , pp. 71-78
    • Kelly, B.M.1    Yu, C.Z.2    Chang, P.L.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0014429243 scopus 로고
    • Cerebroside 3-sulfate as a physiological substrate of arylsulfatase a
    • Mehl E, Jatzkewitz H (1968) Cerebroside 3-sulfate as a physiological substrate of arylsulfatase A. Biochim Biophys Acta 151:619-627
    • (1968) Biochim Biophys Acta , vol.151 , pp. 619-627
    • Mehl, E.1    Jatzkewitz, H.2
  • 25
    • 0029870380 scopus 로고    scopus 로고
    • Chromatin reorganization in rat spermatids during the disappearance of testis-specific histone, H1t, and the appearance of transition proteins TP1 and TP2
    • Oko RJ, Jando V, Wagner CL, Kistler WS, Hermo LS (1996) Chromatin reorganization in rat spermatids during the disappearance of testis-specific histone, H1t, and the appearance of transition proteins TP1 and TP2. Biol Reprod 54:1141-1157
    • (1996) Biol Reprod , vol.54 , pp. 1141-1157
    • Oko, R.J.1    Jando, V.2    Wagner, C.L.3    Kistler, W.S.4    Hermo, L.S.5
  • 26
    • 0037404514 scopus 로고    scopus 로고
    • Structural modifications of the hamster sperm acrosome during post-testicular development in the epididymis
    • Olson GE, Winfrey VP, NagDas SK (2003) Structural modifications of the hamster sperm acrosome during post-testicular development in the epididymis. Microsc Res Tech 61:46-55
    • (2003) Microsc Res Tech , vol.61 , pp. 46-55
    • Olson, G.E.1    Winfrey, V.P.2    NagDas, S.K.3
  • 27
    • 0000972038 scopus 로고
    • Efferent ducts, epididymis, and vas deferens: Structure, functions, and their regulation
    • Knobil E, Neill JD (eds) Raven, New York
    • Robaire B, Hermo L (1988) Efferent ducts, epididymis, and vas deferens: structure, functions, and their regulation. In: Knobil E, Neill JD (eds) The physiology of reproduction. Raven, New York, pp 999-1080
    • (1988) The Physiology of Reproduction , pp. 999-1080
    • Robaire, B.1    Hermo, L.2
  • 29
    • 0031829606 scopus 로고    scopus 로고
    • Maturation of spermatozoa: Modifications of the acrosome and plasma membrane leading to fertilization
    • Toshimori K (1998) Maturation of spermatozoa: modifications of the acrosome and plasma membrane leading to fertilization. Cell Tissue Res 293:177-187
    • (1998) Cell Tissue Res , vol.293 , pp. 177-187
    • Toshimori, K.1
  • 30
    • 0009482260 scopus 로고
    • Electrophoresis transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoresis transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications. Proc Natl Acad Sci USA 76:4350
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 31
    • 1542284264 scopus 로고    scopus 로고
    • 2+- triggered membrane fusion in somatic cells and viruses?
    • 2+-triggered membrane fusion in somatic cells and viruses? Bioessays 26:281-290
    • (2004) Bioessays , vol.26 , pp. 281-290
    • Tulsiani, D.R.P.1    Abou-Haila, A.2
  • 34
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neill JD (eds) Raven, New York
    • Yanagimachi R (1994) Mammalian fertilization. In: Knobil E, Neill JD (eds) The physiology of reproduction. Raven, New York, pp 189-317
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 35
    • 0037404530 scopus 로고    scopus 로고
    • Organization and modifications of sperm acrosome molecules during spermatogenesis and epididymal maturation
    • Yoshinaka K, Toshimori K (2003) Organization and modifications of sperm acrosome molecules during spermatogenesis and epididymal maturation. Microsc Res Tech 61:39-45
    • (2003) Microsc Res Tech , vol.61 , pp. 39-45
    • Yoshinaka, K.1    Toshimori, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.